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Abstract
Since the licensing of the first monoclonal antibody therapy in 1986, monoclonal antibodies have become the largest class of biopharmaceuticals with over 80 antibodies currently approved for a variety of disease indications. The development of smaller, antigen binding antibody fragments, derived from conventional antibodies or produced recombinantly, has been growing at a fast pace. Antibody fragments can be used on their own or linked to other molecules to generate numerous possibilities for bispecific, multi-specific, multimeric, or multifunctional molecules, and to achieve a variety of biological effects. They offer several advantages over full-length monoclonal antibodies, particularly a lower cost of goods, and because of their small size they can penetrate tissues, access challenging epitopes, and have potentially reduced immunogenicity. In this review, we will discuss the structure, production, and mechanism of action of EMA/FDA-approved fragments and of those in clinical and pre-clinical development. We will also discuss current topics of interest surrounding the potential use of antibody fragments for intracellular targeting and blood–brain barrier (BBB) penetration.
Highlights
Since the licensing of the first monoclonal antibody therapy, OrthocloneTM (OKT3), in 1986, the specificity, flexibility, and diversity of antibodies and antibody derivatives has led to their becoming the largest class of biopharmaceuticals [1]
As the VL and VH coding sequences are genetically linked in a single transcript, there is no need to balance the expression of the light chain (LC) and heavy chain (HC)
It was composed of exendin-4, a GLP-1 mimetic peptide isolated from Gila monster saliva, linked to an anti-human serum albumin (HSA) Domain antibodies (dAbs) as a single transcript
Summary
Since the licensing of the first monoclonal antibody (mAb) therapy, OrthocloneTM (OKT3), in 1986, the specificity, flexibility, and diversity of antibodies and antibody derivatives has led to their becoming the largest class of biopharmaceuticals [1]. Over 500 more, including 2nd generation products and novel antibody formats, are currently in clinical trials around the world [1,2,3]. Antibody fragments can offer several advantages over the use of conventional antibodies. They can be produced generally using microbial expression systems, which results in faster cultivation, higher yields, and lower production costs [5]. Their small size allows access to challenging, cryptic epitopes, and tumour penetration, they have reduced immunogenicity, and the lack of Fc limits bystander activation of the immune system [6]. We discuss some of the formats currently being tested in clinical and non-clinical settings, as well as briefly touching on future applications of this expanding class of biopharmaceuticals
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